TY - JOUR
T1 - Nebulin
T2 - The nebulous, multifunctional giant of striated muscle
AU - McElhinny, Abigail S.
AU - Kazmierski, Steven T.
AU - Labeit, Siegfried
AU - Gregorio, Carol C.
N1 - Funding Information:
The authors would like to thank Ryan Mudry for preparation of the figures. They also gratefully acknowledge Carina Wallgren-Pettersson and Katarina Pelin (Department of Medical Genetics, University of Helsinki and Folkhalsan Institute of Genetics) for sharing unpublished data and critical reading of the manuscript. This work was supported by the National Institutes of Health HL57461, HL63926, and HL03985 (to C.C.G.); HL07249 (to S.T.K.), the American Heart Association 0120586Z (to A.S.M.); and the Deutsche Forschungsgemeinschaft (La668/7-1) (to S.L.).
PY - 2003/7
Y1 - 2003/7
N2 - Nebulin is a giant, modular sarcomeric protein and although it was discovered over 2 decades ago, it remains one of the most nebulous components of striated muscle. Previously, several groups identified nebulin as the prime candidate molecule for functioning as a "ruler" to specify the precise lengths of the actin (thin) filaments in skeletal muscle, yet this proposal has never been proven. This article reviews the evidence implicating nebulin as a thin filament ruler, including the most recent studies highlighting its potentially extensive isoform diversity and exciting reports revealing its expression in cardiac tissue. Also examined are novel findings indicating that nebulin is actually a multifunctional filament system, perhaps playing roles in signal transduction, contractile regulation, and myofibril force generation; these ideas are especially intriguing given the growing number of mutations in this giant molecule that are associated with human myopathies.
AB - Nebulin is a giant, modular sarcomeric protein and although it was discovered over 2 decades ago, it remains one of the most nebulous components of striated muscle. Previously, several groups identified nebulin as the prime candidate molecule for functioning as a "ruler" to specify the precise lengths of the actin (thin) filaments in skeletal muscle, yet this proposal has never been proven. This article reviews the evidence implicating nebulin as a thin filament ruler, including the most recent studies highlighting its potentially extensive isoform diversity and exciting reports revealing its expression in cardiac tissue. Also examined are novel findings indicating that nebulin is actually a multifunctional filament system, perhaps playing roles in signal transduction, contractile regulation, and myofibril force generation; these ideas are especially intriguing given the growing number of mutations in this giant molecule that are associated with human myopathies.
UR - http://www.scopus.com/inward/record.url?scp=0038353769&partnerID=8YFLogxK
U2 - 10.1016/S1050-1738(03)00076-8
DO - 10.1016/S1050-1738(03)00076-8
M3 - Review article
C2 - 12837582
AN - SCOPUS:0038353769
SN - 1050-1738
VL - 13
SP - 195
EP - 201
JO - Trends in Cardiovascular Medicine
JF - Trends in Cardiovascular Medicine
IS - 5
ER -